Premium
ARGININE DECARBOXYLASE IMMOBILIZATION
Author(s) -
VALLEVEGA P.,
YOUNG CLYDE T.,
SWAISGOOD H. E.
Publication year - 1980
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1980.tb07522.x
Subject(s) - glutaraldehyde , immobilized enzyme , covalent bond , chemistry , enzyme , arginine , chromatography , derivative (finance) , lysine decarboxylase , nuclear chemistry , biochemistry , organic chemistry , amino acid , putrescine , financial economics , cadaverine , economics
Arginine decarboxylase was immobilized by (1) glutaraldehyde crosslinking to form a gel, (2) chemical coupling to a glutaraldehyde derivative of alkylaminopropyl glass, or (3) chemical coupling to succinamidopropyl glass beads. Enzyme activity was tested by either the enzyme electrode system or enzyme reactor system. Covalent coupling to alkylaminopropyl glass appeared to be the best immobilization procedure. The best detection procedure was the enzyme reactor (linear range 3 × 10 −4 to 3 × 10 −3 M, linear equation mV = 53.43 log[Arg] + 226.38). Equilibrium was attained in 4–6 min with the enzyme reactor.